Structure of PDB 6lge Chain B Binding Site BS02

Receptor Information
>6lge Chain B (length=569) Species: 7091 (Bombyx mori) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PPTEVIQLDWWKNCVLYQIYPRSFKDSDGDGIGDLKGIISELKHFVDAGV
DAIWMSPIFESPMVDFGYDISNFYDIHYEYGTMEDFEELLDKAHELGLKV
LLDFVPNHASNESEYFIKSEAREPGYENFFIWADPLPNPENPGVRLPPSN
WVSQFGGSAWEWSEKRQQYYLHQFAIQQVDFDFRNPAVKQEMFNIMKFWL
DKGADGFRLDALPYLIEADPADHEGRYPDDPLSGLTQFESHQLGYTIPLY
TKDLIELYDVVYEWREFLDEYNKNHGGDTRVVFSEGYANVSMTMLYYGNE
DGAIGAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFGN
HDNNRMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDTV
DIEACNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDYQ
EINLAKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVRS
LPTHDTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEIT
SSQLSLEAGEALVLKAQPI
Ligand information
Ligand IDGLC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6+/m1/s1
InChIKeyWQZGKKKJIJFFOK-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-glucopyranose;
alpha-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL423707
DrugBank
ZINCZINC000003861213
PDB chain6lge Chain D Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6lge Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
Resolution1.75 Å
Binding residue
(original residue number in PDB)		Y324 N390
Binding residue
(residue number reindexed from 1)		Y287 N353
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D140 D247 E322 H388 D389
Catalytic site (residue number reindexed from 1) D103 D210 E285 H351 D352
Enzyme Commision number 3.2.1.20: alpha-glucosidase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6lge, PDBe:6lge, PDBj:6lge
PDBsum6lge
PubMed32381508
UniProtA0A077JI83

[Back to BioLiP]